dbPTM

RPB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPB1_HUMAN
UniProt AC	P24928
Protein Name	DNA-directed RNA polymerase II subunit RPB1
Gene Name	POLR2A
Organism	Homo sapiens (Human).
Sequence Length	1970
Subcellular Localization	Nucleus . Cytoplasm . Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear.
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD. [PubMed: 24207025 Methylation and dimethylation have a repressive effect on target genes expression (By similarity; (Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.]
Protein Sequence	MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MHGGGPPS -------CCCCCCCC	31.36	19413330
8	Phosphorylation	MHGGGPPSGDSACPL CCCCCCCCCCCCCCC	59.37	25159151
27	Phosphorylation	RVQFGVLSPDELKRM EEEEEECCHHHHHHC	28.09	25159151
32	Ubiquitination	VLSPDELKRMSVTEG ECCHHHHHHCEECCC	43.96	21906983
35	Phosphorylation	PDELKRMSVTEGGIK HHHHHHCEECCCCCC	29.89	30576142
37	Phosphorylation	ELKRMSVTEGGIKYP HHHHCEECCCCCCCC	22.93	30576142
42	Ubiquitination	SVTEGGIKYPETTEG EECCCCCCCCCCCCC	59.01	21890473
42	Acetylation	SVTEGGIKYPETTEG EECCCCCCCCCCCCC	59.01	26051181
42	Ubiquitination	SVTEGGIKYPETTEG EECCCCCCCCCCCCC	59.01	22817900
42	Ubiquitination	SVTEGGIKYPETTEG EECCCCCCCCCCCCC	59.01	21890473
46	Phosphorylation	GGIKYPETTEGGRPK CCCCCCCCCCCCCCC	26.16	-
47	Phosphorylation	GIKYPETTEGGRPKL CCCCCCCCCCCCCCC	30.85	30576142
92	Ubiquitination	FGHIELAKPVFHVGF CCHHEECCCCEEHHH	55.10	-
116	Ubiquitination	CVCFFCSKLLVDSNN HHHHHHHHHHHCCCC	47.20	21963094
121	Phosphorylation	CSKLLVDSNNPKIKD HHHHHHCCCCHHHHH	30.90	28188228
125	Ubiquitination	LVDSNNPKIKDILAK HHCCCCHHHHHHHHH	65.59	29967540
127	Ubiquitination	DSNNPKIKDILAKSK CCCCHHHHHHHHHCC	44.86	29967540
132	Ubiquitination	KIKDILAKSKGQPKK HHHHHHHHCCCCCCC	49.62	27667366
134	Acetylation	KDILAKSKGQPKKRL HHHHHHCCCCCCCCC	61.94	68701
139	Acetylation	KSKGQPKKRLTHVYD HCCCCCCCCCCHHHH	60.36	68705
145	Phosphorylation	KKRLTHVYDLCKGKN CCCCCHHHHHHCCCC	8.80	28152594
149	Ubiquitination	THVYDLCKGKNICEG CHHHHHHCCCCCCCC	79.00	21963094
151	Ubiquitination	VYDLCKGKNICEGGE HHHHHCCCCCCCCCC	28.74	21963094
163	Ubiquitination	GGEEMDNKFGVEQPE CCCCCCCCCCCCCCC	38.95	21963094
176	Phosphorylation	PEGDEDLTKEKGHGG CCCCCCCHHHCCCCC	49.86	23312004
177	Acetylation	EGDEDLTKEKGHGGC CCCCCCHHHCCCCCC	65.80	26051181
177	Ubiquitination	EGDEDLTKEKGHGGC CCCCCCHHHCCCCCC	65.80	21906983
179	Ubiquitination	DEDLTKEKGHGGCGR CCCCHHHCCCCCCCC	58.73	22817900
199	Phosphorylation	RRSGLELYAEWKHVN HHCCCCEEEEEECCC	7.97	27642862
203	Ubiquitination	LELYAEWKHVNEDSQ CCEEEEEECCCCCHH	29.22	-
209	Phosphorylation	WKHVNEDSQEKKILL EECCCCCHHHCEECC	33.78	28985074
212	Ubiquitination	VNEDSQEKKILLSPE CCCCHHHCEECCCHH	37.16	-
213	Sumoylation	NEDSQEKKILLSPER CCCHHHCEECCCHHH	37.52	-
213	Sumoylation	NEDSQEKKILLSPER CCCHHHCEECCCHHH	37.52	-
213	Ubiquitination	NEDSQEKKILLSPER CCCHHHCEECCCHHH	37.52	22505724
217	Phosphorylation	QEKKILLSPERVHEI HHCEECCCHHHHHHH	22.67	25159151
226	Ubiquitination	ERVHEIFKRISDEEC HHHHHHHHHCCHHHC	55.26	29967540
233	Glutathionylation	KRISDEECFVLGMEP HHCCHHHCEECCCCC	2.41	22555962
269	Phosphorylation	PAVVMQGSARNQDDL CEEEECCCCCCHHHH	13.73	21406692
279	Ubiquitination	NQDDLTHKLADIVKI CHHHHHHHHHHHHHH	39.89	21906983
285	Acetylation	HKLADIVKINNQLRR HHHHHHHHHHHHHHH	39.80	20167786
285	Ubiquitination	HKLADIVKINNQLRR HHHHHHHHHHHHHHH	39.80	21906983
331	Ubiquitination	GLPRAMQKSGRPLKS CHHHHHHHCCCCCHH	41.62	29967540
337	Ubiquitination	QKSGRPLKSLKQRLK HHCCCCCHHHHHHHC	57.32	21963094
340	Ubiquitination	GRPLKSLKQRLKGKE CCCCHHHHHHHCCCC	40.23	22817900
357	Acetylation	VRGNLMGKRVDFSAR CCCCCCCCCCCCCCC	34.97	25953088
368	Phosphorylation	FSARTVITPDPNLSI CCCCEEECCCCCCCH	19.80	-
374	Phosphorylation	ITPDPNLSIDQVGVP ECCCCCCCHHHCCCC	30.66	28348404
417	Ubiquitination	NSQYPGAKYIIRDNG CCCCCCCEEEEEECC	42.78	21906983
426	Methylation	IIRDNGDRIDLRFHP EEEECCCEEEEEECC	26.22	115488141
434	Ubiquitination	IDLRFHPKPSDLHLQ EEEEECCCCCCCCCC	48.89	29967540
445	Ubiquitination	LHLQTGYKVERHMCD CCCCCCCEEEEEECC	38.68	27667366
451	Glutathionylation	YKVERHMCDGDIVIF CEEEEEECCCCEEEE	4.29	22555962
466	Ubiquitination	NRQPTLHKMSMMGHR CCCCCCHHHHHCCCC	35.46	-
481	Phosphorylation	VRILPWSTFRLNLSV EEECCCCCEEEEEEE	14.65	30387612
520	Sulfoxidation	AEIQELAMVPRMIVT HHHHHHHCCCEEEEC	7.15	21406390
530	Phosphorylation	RMIVTPQSNRPVMGI EEEECCCCCCCCCEE	35.69	-
543	Phosphorylation	GIVQDTLTAVRKFTK EECHHHHHHHHHHCC	25.79	-
549	Phosphorylation	LTAVRKFTKRDVFLE HHHHHHHCCCCCHHH	28.36	-
581	Ubiquitination	VPQPAILKPRPLWTG CCCCCCCCCCCCCCC	32.63	27667366
587	Phosphorylation	LKPRPLWTGKQIFSL CCCCCCCCCCHHHHE	42.03	-
607	Phosphorylation	INCIRTHSTHPDDED EEEEECCCCCCCCCC	28.00	24247654
608	Phosphorylation	NCIRTHSTHPDDEDS EEEECCCCCCCCCCC	29.80	-
618	Phosphorylation	DDEDSGPYKHISPGD CCCCCCCCCCCCCCC	20.80	27642862
619	Acetylation	DEDSGPYKHISPGDT CCCCCCCCCCCCCCE	37.28	25953088
619	Ubiquitination	DEDSGPYKHISPGDT CCCCCCCCCCCCCCE	37.28	21906983
627	Ubiquitination	HISPGDTKVVVENGE CCCCCCEEEEEECCE	37.46	21963094
642	Acetylation	LIMGILCKKSLGTSA EEEEEEECCCCCCCC	41.79	25953088
642	Ubiquitination	LIMGILCKKSLGTSA EEEEEEECCCCCCCC	41.79	21963094
643	Ubiquitination	IMGILCKKSLGTSAG EEEEEECCCCCCCCC	50.33	22817900
697	Ubiquitination	GDSIADSKTYQDIQN CCHHHCCCHHHHHHH	52.37	-
698	Phosphorylation	DSIADSKTYQDIQNT CHHHCCCHHHHHHHH	30.30	-
699	Phosphorylation	SIADSKTYQDIQNTI HHHCCCHHHHHHHHH	14.13	27642862
707	Ubiquitination	QDIQNTIKKAKQDVI HHHHHHHHHHHHHHH	44.64	21890473
707	Sumoylation	QDIQNTIKKAKQDVI HHHHHHHHHHHHHHH	44.64	-
707	Sumoylation	QDIQNTIKKAKQDVI HHHHHHHHHHHHHHH	44.64	-
707	Ubiquitination	QDIQNTIKKAKQDVI HHHHHHHHHHHHHHH	44.64	21906983
707	Ubiquitination	QDIQNTIKKAKQDVI HHHHHHHHHHHHHHH	44.64	21890473
708	Methylation	DIQNTIKKAKQDVIE HHHHHHHHHHHHHHH	57.89	-
708	Ubiquitination	DIQNTIKKAKQDVIE HHHHHHHHHHHHHHH	57.89	21963094
710	Sumoylation	QNTIKKAKQDVIEVI HHHHHHHHHHHHHHH	56.78	-
710	Acetylation	QNTIKKAKQDVIEVI HHHHHHHHHHHHHHH	56.78	88941
710	Sumoylation	QNTIKKAKQDVIEVI HHHHHHHHHHHHHHH	56.78	-
710	Ubiquitination	QNTIKKAKQDVIEVI HHHHHHHHHHHHHHH	56.78	21906983
719	Ubiquitination	DVIEVIEKAHNNELE HHHHHHHHHHHCCCC	43.77	21906983
732	Phosphorylation	LEPTPGNTLRQTFEN CCCCCCCHHHHHHHH	29.27	-
736	Phosphorylation	PGNTLRQTFENQVNR CCCHHHHHHHHHHHH	26.87	18452278
751	Ubiquitination	ILNDARDKTGSSAQK HHHHHHHHCCCHHHH	49.59	21890473
751	Ubiquitination	ILNDARDKTGSSAQK HHHHHHHHCCCHHHH	49.59	21963094
751	Ubiquitination	ILNDARDKTGSSAQK HHHHHHHHCCCHHHH	49.59	21890473
758	Ubiquitination	KTGSSAQKSLSEYNN HCCCHHHHHHHHHHC	53.75	21890473
758	Ubiquitination	KTGSSAQKSLSEYNN HCCCHHHHHHHHHHC	53.75	23000965
758	Ubiquitination	KTGSSAQKSLSEYNN HCCCHHHHHHHHHHC	53.75	21890473
759	Phosphorylation	TGSSAQKSLSEYNNF CCCHHHHHHHHHHCC	25.66	26330541
761	Phosphorylation	SSAQKSLSEYNNFKS CHHHHHHHHHHCCCH	45.16	26330541
763	Phosphorylation	AQKSLSEYNNFKSMV HHHHHHHHHCCCHHH	16.42	26330541
767	Ubiquitination	LSEYNNFKSMVVSGA HHHHHCCCHHHHHCC	39.50	21890473
767	Methylation	LSEYNNFKSMVVSGA HHHHHCCCHHHHHCC	39.50	30790047
767	Ubiquitination	LSEYNNFKSMVVSGA HHHHHCCCHHHHHCC	39.50	21906983
767	Ubiquitination	LSEYNNFKSMVVSGA HHHHHCCCHHHHHCC	39.50	21890473
768	Phosphorylation	SEYNNFKSMVVSGAK HHHHCCCHHHHHCCC	16.81	-
772	Phosphorylation	NFKSMVVSGAKGSKI CCCHHHHHCCCCCCE	22.94	22817900
775	Ubiquitination	SMVVSGAKGSKINIS HHHHHCCCCCCEEHH	68.21	21906983
777	Phosphorylation	VVSGAKGSKINISQV HHHCCCCCCEEHHHE	29.65	22817900
778	Ubiquitination	VSGAKGSKINISQVI HHCCCCCCEEHHHEE	48.73	22817900
796	Ubiquitination	GQQNVEGKRIPFGFK ECCCCCCCCCCCCCC	33.38	21890473
796	Ubiquitination	GQQNVEGKRIPFGFK ECCCCCCCCCCCCCC	33.38	21906983
796	Ubiquitination	GQQNVEGKRIPFGFK ECCCCCCCCCCCCCC	33.38	21890473
803	Acetylation	KRIPFGFKHRTLPHF CCCCCCCCCCCCCCC	32.34	26051181
803	Methylation	KRIPFGFKHRTLPHF CCCCCCCCCCCCCCC	32.34	115975325
803	Ubiquitination	KRIPFGFKHRTLPHF CCCCCCCCCCCCCCC	32.34	29967540
812	Ubiquitination	RTLPHFIKDDYGPES CCCCCCCCCCCCCCC	43.53	21890473
812	Acetylation	RTLPHFIKDDYGPES CCCCCCCCCCCCCCC	43.53	26051181
812	Ubiquitination	RTLPHFIKDDYGPES CCCCCCCCCCCCCCC	43.53	21963094
812	Ubiquitination	RTLPHFIKDDYGPES CCCCCCCCCCCCCCC	43.53	21890473
853	Ubiquitination	GLIDTAVKTAETGYI CHHHHHHHHCHHHHH	39.28	21906983
857	Phosphorylation	TAVKTAETGYIQRRL HHHHHCHHHHHHHHH	32.59	28152594
859	Phosphorylation	VKTAETGYIQRRLIK HHHCHHHHHHHHHHH	10.99	28152594
866	Ubiquitination	YIQRRLIKSMESVMV HHHHHHHHHHHHHHH	48.63	21890473
866	Ubiquitination	YIQRRLIKSMESVMV HHHHHHHHHHHHHHH	48.63	21906983
866	Ubiquitination	YIQRRLIKSMESVMV HHHHHHHHHHHHHHH	48.63	21890473
867	Phosphorylation	IQRRLIKSMESVMVK HHHHHHHHHHHHHHH	22.31	21406692
870	Phosphorylation	RLIKSMESVMVKYDA HHHHHHHHHHHHCCH	13.58	21406692
874	Ubiquitination	SMESVMVKYDATVRN HHHHHHHHCCHHHHH	21.22	21906983
875	Phosphorylation	MESVMVKYDATVRNS HHHHHHHCCHHHHHH	10.21	29978859
878	Phosphorylation	VMVKYDATVRNSINQ HHHHCCHHHHHHHHH	19.66	29978859
882	Phosphorylation	YDATVRNSINQVVQL CCHHHHHHHHHEEEE	16.61	29978859
910	Acetylation	FQNLATLKPSNKAFE EECCCCCCCCCHHHH	41.88	26051181
910	Ubiquitination	FQNLATLKPSNKAFE EECCCCCCCCCHHHH	41.88	21906983
914	Ubiquitination	ATLKPSNKAFEKKFR CCCCCCCHHHHHHHC	59.81	21906983
918	Ubiquitination	PSNKAFEKKFRFDYT CCCHHHHHHHCCCCC	51.24	21906983
919	Ubiquitination	SNKAFEKKFRFDYTN CCHHHHHHHCCCCCC	34.28	22817900
940	Acetylation	TLQEDLVKDVLSNAH HHHHHHHHHHHHHHH	49.79	26051181
940	Ubiquitination	TLQEDLVKDVLSNAH HHHHHHHHHHHHHHH	49.79	21906983
972	Phosphorylation	VLRVIFPTGDSKVVL EEEEEECCCCCCEEE	42.76	21406692
975	Phosphorylation	VIFPTGDSKVVLPCN EEECCCCCCEEEEHH	28.79	21406692
976	Ubiquitination	IFPTGDSKVVLPCNL EECCCCCCEEEEHHH	40.89	21963094
992	Ubiquitination	RMIWNAQKIFHINPR HHHHHHHHHEECCCC	44.95	21963094
1008	Ubiquitination	PSDLHPIKVVEGVKE CCCCCCCEEHHHHHH	44.68	21890473
1008	Acetylation	PSDLHPIKVVEGVKE CCCCCCCEEHHHHHH	44.68	26051181
1008	Ubiquitination	PSDLHPIKVVEGVKE CCCCCCCEEHHHHHH	44.68	23000965
1008	Ubiquitination	PSDLHPIKVVEGVKE CCCCCCCEEHHHHHH	44.68	21890473
1014	Acetylation	IKVVEGVKELSKKLV CEEHHHHHHHHCCEE	64.89	27452117
1014	Ubiquitination	IKVVEGVKELSKKLV CEEHHHHHHHHCCEE	64.89	23000965
1018	Ubiquitination	EGVKELSKKLVIVNG HHHHHHHCCEEEECC	63.85	22817900
1019	Ubiquitination	GVKELSKKLVIVNGD HHHHHHCCEEEECCC	44.61	21906983
1030	Phosphorylation	VNGDDPLSRQAQENA ECCCCHHHHHHHHHH	27.95	27732954
1109	Phosphorylation	MTLNTFHYAGVSAKN CEEECHHHCCCCCCC	10.81	22817900
1125	Ubiquitination	TLGVPRLKELINISK EECCCCHHHHHCCCC	52.32	21890473
1125	Ubiquitination	TLGVPRLKELINISK EECCCCHHHHHCCCC	52.32	21906983
1125	Ubiquitination	TLGVPRLKELINISK EECCCCHHHHHCCCC	52.32	21890473
1132	Ubiquitination	KELINISKKPKTPSL HHHHCCCCCCCCCCE	70.11	21963094
1133	Ubiquitination	ELINISKKPKTPSLT HHHCCCCCCCCCCEE	44.98	22817900
1135	Ubiquitination	INISKKPKTPSLTVF HCCCCCCCCCCEEEE	80.22	22817900
1138	Phosphorylation	SKKPKTPSLTVFLLG CCCCCCCCEEEEECC	41.73	30278072
1147	Phosphorylation	TVFLLGQSARDAERA EEEECCCCHHHHHHH	24.39	30278072
1155	Ubiquitination	ARDAERAKDILCRLE HHHHHHHHHHHHHCC	52.07	29967540
1225	Sumoylation	RKHMTDRKLTMEQIA CCCCCCCCCCHHHHH	51.63	-
1225	2-Hydroxyisobutyrylation	RKHMTDRKLTMEQIA CCCCCCCCCCHHHHH	51.63	-
1225	Sumoylation	RKHMTDRKLTMEQIA CCCCCCCCCCHHHHH	51.63	-
1225	Ubiquitination	RKHMTDRKLTMEQIA CCCCCCCCCCHHHHH	51.63	21906983
1234	Ubiquitination	TMEQIAEKINAGFGD CHHHHHHHHHCCCCC	32.04	29967540
1254	Ubiquitination	FNDDNAEKLVLRIRI ECCCCHHHHEEEEEE	41.29	21963094
1268	Ubiquitination	IMNSDENKMQEEEEV ECCCCCCHHHHHHHH	39.65	21906983
1278	Ubiquitination	EEEEVVDKMDDDVFL HHHHHHHHCCHHHHH	32.40	21906983
1287	Glutathionylation	DDDVFLRCIESNMLT CHHHHHHHHHHCCCC	4.38	22555962
1308	Phosphorylation	IEQISKVYMHLPQTD HHHHHHHHHCCCCCC	5.20	27642862
1317	Ubiquitination	HLPQTDNKKKIIITE CCCCCCCCCEEEECC	59.25	23000965
1318	Ubiquitination	LPQTDNKKKIIITED CCCCCCCCEEEECCC	56.30	23000965
1319	Ubiquitination	PQTDNKKKIIITEDG CCCCCCCEEEECCCC	40.52	23000965
1348	Phosphorylation	VSLMRVLSEKDVDPV CCCCHHHHCCCCCCC	39.48	26714015
1350	Acetylation	LMRVLSEKDVDPVRT CCHHHHCCCCCCCCC	60.73	26051181
1350	Ubiquitination	LMRVLSEKDVDPVRT CCHHHHCCCCCCCCC	60.73	21906983
1383	Phosphorylation	KALERELYHVISFDG HHHHHHCCEEEECCC	6.84	-
1387	Phosphorylation	RELYHVISFDGSYVN HHCCEEEECCCCCCC	19.05	28152594
1391	Phosphorylation	HVISFDGSYVNYRHL EEEECCCCCCCHHHH	27.96	28152594
1392	Phosphorylation	VISFDGSYVNYRHLA EEECCCCCCCHHHHH	9.76	28152594
1395	Phosphorylation	FDGSYVNYRHLALLC CCCCCCCHHHHHHHH	6.86	28152594
1406	Phosphorylation	ALLCDTMTCRGHLMA HHHHHCEECCCHHHH	10.92	-
1415	Phosphorylation	RGHLMAITRHGVNRQ CCHHHHHHCCCCCCC	13.69	21406692
1424	Phosphorylation	HGVNRQDTGPLMKCS CCCCCCCCCCCCCCC	32.15	-
1429	Ubiquitination	QDTGPLMKCSFEETV CCCCCCCCCCHHHHH	34.12	21963094
1479	Ubiquitination	DLLLDAEKCKYGMEI HHHCCHHHCCCCCCC	37.43	21963094
1481	Ubiquitination	LLDAEKCKYGMEIPT HCCHHHCCCCCCCCC	56.77	22817900
1505	Phosphorylation	PTGMFFGSAPSPMGG CCCEECCCCCCCCCC	31.67	26074081
1508	Phosphorylation	MFFGSAPSPMGGISP EECCCCCCCCCCCCC	27.51	26074081
1514	Phosphorylation	PSPMGGISPAMTPWN CCCCCCCCCCCCCCC	15.19	26074081
1518	Phosphorylation	GGISPAMTPWNQGAT CCCCCCCCCCCCCCC	27.53	26074081
1525	Phosphorylation	TPWNQGATPAYGAWS CCCCCCCCCCCCCCC	18.44	-
1532	Phosphorylation	TPAYGAWSPSVGSGM CCCCCCCCCCCCCCC	13.53	26074081
1534	O-linked_Glycosylation	AYGAWSPSVGSGMTP CCCCCCCCCCCCCCC	33.33	26807597
1534	Phosphorylation	AYGAWSPSVGSGMTP CCCCCCCCCCCCCCC	33.33	26074081
1540	Phosphorylation	PSVGSGMTPGAAGFS CCCCCCCCCCCCCCC	23.30	-
1568	Phosphorylation	YSPAWSPTPGSPGSP CCCCCCCCCCCCCCC	34.46	26074081
1571	Phosphorylation	AWSPTPGSPGSPGPS CCCCCCCCCCCCCCC	27.56	26074081
1574	Phosphorylation	PTPGSPGSPGPSSPY CCCCCCCCCCCCCCC	30.02	26074081
1590	Phosphorylation	PSPGGAMSPSYSPTS CCCCCCCCCCCCCCC	15.34	25137130
1592	Phosphorylation	PGGAMSPSYSPTSPA CCCCCCCCCCCCCCC	30.82	25137130
1594	Phosphorylation	GAMSPSYSPTSPAYE CCCCCCCCCCCCCCC	26.49	25137130
1597	Phosphorylation	SPSYSPTSPAYEPRS CCCCCCCCCCCCCCC	15.77	25137130
1603	Methylation	TSPAYEPRSPGGYTP CCCCCCCCCCCCCCC	43.47	26700805
1615	Phosphorylation	YTPQSPSYSPTSPSY CCCCCCCCCCCCCCC	23.27	-
1616	Phosphorylation	TPQSPSYSPTSPSYS CCCCCCCCCCCCCCC	26.49	16672643
1618	O-linked_Glycosylation	QSPSYSPTSPSYSPT CCCCCCCCCCCCCCC	47.53	50084999
1618	Phosphorylation	QSPSYSPTSPSYSPT CCCCCCCCCCCCCCC	47.53	22053051
1619	O-linked_Glycosylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	26807597
1619	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	19901026
1621	O-linked_Glycosylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	26807597
1621	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	18079404
1626	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1647	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1649	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1654	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1656	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1661	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1663	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1668	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1670	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1675	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1677	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1682	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1684	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1689	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1691	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1696	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1698	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1703	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1705	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1710	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1712	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1717	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1719	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1724	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1726	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1731	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1733	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1738	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1766	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1794	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	12721286
1796	Phosphorylation	SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC	37.70	-
1810	Asymmetric dimethylarginine	SYSPSSPRYTPQSPT CCCCCCCCCCCCCCC	50.32	-
1810	Methylation	SYSPSSPRYTPQSPT CCCCCCCCCCCCCCC	50.32	26700805
1811	Phosphorylation	YSPSSPRYTPQSPTY CCCCCCCCCCCCCCC	26.59	-
1812	Phosphorylation	SPSSPRYTPQSPTYT CCCCCCCCCCCCCCC	19.01	23186163
1815	Phosphorylation	SPRYTPQSPTYTPSS CCCCCCCCCCCCCCC	22.03	22817900
1817	Phosphorylation	RYTPQSPTYTPSSPS CCCCCCCCCCCCCCC	45.32	24719451
1818	Phosphorylation	YTPQSPTYTPSSPSY CCCCCCCCCCCCCCC	21.75	23186163
1819	Phosphorylation	TPQSPTYTPSSPSYS CCCCCCCCCCCCCCC	21.12	24719451
1821	Phosphorylation	QSPTYTPSSPSYSPS CCCCCCCCCCCCCCC	47.26	27251275
1822	Phosphorylation	SPTYTPSSPSYSPSS CCCCCCCCCCCCCCC	21.04	27251275
1824	Phosphorylation	TYTPSSPSYSPSSPS CCCCCCCCCCCCCCC	39.94	27251275
1825	Phosphorylation	YTPSSPSYSPSSPSY CCCCCCCCCCCCCCC	28.16	27251275
1826	Phosphorylation	TPSSPSYSPSSPSYS CCCCCCCCCCCCCCC	23.73	-
1828	Phosphorylation	SSPSYSPSSPSYSPA CCCCCCCCCCCCCCC	49.27	-
1829	Phosphorylation	SPSYSPSSPSYSPAS CCCCCCCCCCCCCCC	22.65	27251275
1831	Phosphorylation	SYSPSSPSYSPASPK CCCCCCCCCCCCCCC	39.94	27251275
1832	Phosphorylation	YSPSSPSYSPASPKY CCCCCCCCCCCCCCC	23.27	-
1833	Phosphorylation	SPSSPSYSPASPKYT CCCCCCCCCCCCCCC	20.51	21406692
1836	Phosphorylation	SPSYSPASPKYTPTS CCCCCCCCCCCCCCC	25.88	15302935
1838	Methylation	SYSPASPKYTPTSPS CCCCCCCCCCCCCCC	60.30	-
1839	Phosphorylation	YSPASPKYTPTSPSY CCCCCCCCCCCCCCC	22.72	21945579
1840	Phosphorylation	SPASPKYTPTSPSYS CCCCCCCCCCCCCCC	26.64	23401153
1842	Phosphorylation	ASPKYTPTSPSYSPS CCCCCCCCCCCCCCC	45.53	21945579
1843	Phosphorylation	SPKYTPTSPSYSPSS CCCCCCCCCCCCCCC	17.04	23927012
1845	Phosphorylation	KYTPTSPSYSPSSPE CCCCCCCCCCCCCCC	37.70	23927012
1846	Phosphorylation	YTPTSPSYSPSSPEY CCCCCCCCCCCCCCC	28.16	21945579
1847	Phosphorylation	TPTSPSYSPSSPEYT CCCCCCCCCCCCCCC	23.73	25159151
1849	Phosphorylation	TSPSYSPSSPEYTPT CCCCCCCCCCCCCCC	53.21	23927012
1850	Phosphorylation	SPSYSPSSPEYTPTS CCCCCCCCCCCCCCC	25.74	23927012
1853	Phosphorylation	YSPSSPEYTPTSPKY CCCCCCCCCCCCCCC	22.77	23927012
1854	Phosphorylation	SPSSPEYTPTSPKYS CCCCCCCCCCCCCCC	20.59	21945579
1856	Phosphorylation	SSPEYTPTSPKYSPT CCCCCCCCCCCCCCC	50.27	21945579
1857	Phosphorylation	SPEYTPTSPKYSPTS CCCCCCCCCCCCCCC	22.16	23927012
1859	Acetylation	EYTPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	26051181
1859	Methylation	EYTPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	26566685
1860	Phosphorylation	YTPTSPKYSPTSPKY CCCCCCCCCCCCCCC	24.22	30266825
1861	Phosphorylation	TPTSPKYSPTSPKYS CCCCCCCCCCCCCCC	28.03	30266825
1863	Phosphorylation	TSPKYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	30266825
1864	Phosphorylation	SPKYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	23927012
1866	Acetylation	KYSPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	26566685
1866	Methylation	KYSPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	26566685
1867	Phosphorylation	YSPTSPKYSPTSPKY CCCCCCCCCCCCCCC	24.22	30266825
1868	Phosphorylation	SPTSPKYSPTSPKYS CCCCCCCCCCCCCCC	28.03	23401153
1870	Phosphorylation	TSPKYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	30266825
1871	Phosphorylation	SPKYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	23927012
1873	Acetylation	KYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26051181
1873	Methylation	KYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26566685
1874	Phosphorylation	YSPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	23927012
1875	Phosphorylation	SPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	22167270
1877	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	22167270
1878	Phosphorylation	SPKYSPTSPTYSPTT CCCCCCCCCCCCCCC	20.73	22167270
1880	Phosphorylation	KYSPTSPTYSPTTPK CCCCCCCCCCCCCCC	36.08	22167270
1881	Phosphorylation	YSPTSPTYSPTTPKY CCCCCCCCCCCCCCC	18.94	23927012
1882	Phosphorylation	SPTSPTYSPTTPKYS CCCCCCCCCCCCCCC	20.46	25159151
1884	Phosphorylation	TSPTYSPTTPKYSPT CCCCCCCCCCCCCCC	50.19	23927012
1885	Phosphorylation	SPTYSPTTPKYSPTS CCCCCCCCCCCCCCC	22.59	25159151
1887	Acetylation	TYSPTTPKYSPTSPT CCCCCCCCCCCCCCC	57.16	26566685
1887	Methylation	TYSPTTPKYSPTSPT CCCCCCCCCCCCCCC	57.16	26566685
1888	Phosphorylation	YSPTTPKYSPTSPTY CCCCCCCCCCCCCCC	22.53	21945579
1889	Phosphorylation	SPTTPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	23927012
1891	Phosphorylation	TTPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	25159151
1892	Phosphorylation	TPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	25159151
1894	Phosphorylation	KYSPTSPTYSPTSPV CCCCCCCCCCCCCCC	36.08	25159151
1895	Phosphorylation	YSPTSPTYSPTSPVY CCCCCCCCCCCCCCC	18.94	21945579
1896	Phosphorylation	SPTSPTYSPTSPVYT CCCCCCCCCCCCCCC	24.95	25159151
1898	Phosphorylation	TSPTYSPTSPVYTPT CCCCCCCCCCCCCCC	39.46	25159151
1899	Phosphorylation	SPTYSPTSPVYTPTS CCCCCCCCCCCCCCC	18.76	25159151
1902	Phosphorylation	YSPTSPVYTPTSPKY CCCCCCCCCCCCCCC	15.47	21945579
1903	Phosphorylation	SPTSPVYTPTSPKYS CCCCCCCCCCCCCCC	21.96	21945579
1905	Phosphorylation	TSPVYTPTSPKYSPT CCCCCCCCCCCCCCC	50.27	23927012
1906	Phosphorylation	SPVYTPTSPKYSPTS CCCCCCCCCCCCCCC	22.16	23927012
1908	Acetylation	VYTPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26051181
1908	Methylation	VYTPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	-
1909	Phosphorylation	YTPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	23927012
1910	Phosphorylation	TPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	25159151
1912	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	22167270
1913	Phosphorylation	SPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	22167270
1915	Phosphorylation	KYSPTSPTYSPTSPK CCCCCCCCCCCCCCC	36.08	19664994
1916	Phosphorylation	YSPTSPTYSPTSPKY CCCCCCCCCCCCCCC	18.94	25159151
1917	Phosphorylation	SPTSPTYSPTSPKYS CCCCCCCCCCCCCCC	24.95	22167270
1919	Phosphorylation	TSPTYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	25159151
1920	Phosphorylation	SPTYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	25159151
1922	Acetylation	TYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26566685
1922	Methylation	TYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26566685
1923	Phosphorylation	YSPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	23927012
1924	Phosphorylation	SPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	23927012
1926	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	22167270
1927	Phosphorylation	SPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	22167270
1929	Phosphorylation	KYSPTSPTYSPTSPK CCCCCCCCCCCCCCC	36.08	19664994
1930	Phosphorylation	YSPTSPTYSPTSPKG CCCCCCCCCCCCCCC	18.94	23927012
1931	Phosphorylation	SPTSPTYSPTSPKGS CCCCCCCCCCCCCCC	24.95	22167270
1933	Phosphorylation	TSPTYSPTSPKGSTY CCCCCCCCCCCCCCC	52.28	28176443
1934	Phosphorylation	SPTYSPTSPKGSTYS CCCCCCCCCCCCCCC	28.18	23927012
1936	Acetylation	TYSPTSPKGSTYSPT CCCCCCCCCCCCCCC	66.32	26566685
1936	Methylation	TYSPTSPKGSTYSPT CCCCCCCCCCCCCCC	66.32	26566685
1938	Phosphorylation	SPTSPKGSTYSPTSP CCCCCCCCCCCCCCC	30.23	25159151
1939	Phosphorylation	PTSPKGSTYSPTSPG CCCCCCCCCCCCCCC	36.37	25159151
1940	Phosphorylation	TSPKGSTYSPTSPGY CCCCCCCCCCCCCCC	17.85	21406692
1941	Phosphorylation	SPKGSTYSPTSPGYS CCCCCCCCCCCCCCC	23.07	26074081
1943	Phosphorylation	KGSTYSPTSPGYSPT CCCCCCCCCCCCCCC	41.43	26074081
1944	Phosphorylation	GSTYSPTSPGYSPTS CCCCCCCCCCCCCCC	21.51	26074081
1947	Phosphorylation	YSPTSPGYSPTSPTY CCCCCCCCCCCCCCC	18.17	20873877
1948	Phosphorylation	SPTSPGYSPTSPTYS CCCCCCCCCCCCCCC	27.84	20873877
1950	Phosphorylation	TSPGYSPTSPTYSLT CCCCCCCCCCCCCCC	41.20	20873877
1951	Phosphorylation	SPGYSPTSPTYSLTS CCCCCCCCCCCCCCC	20.73	20873877
1953	Phosphorylation	GYSPTSPTYSLTSPA CCCCCCCCCCCCCCC	26.05	30108239
1954	Phosphorylation	YSPTSPTYSLTSPAI CCCCCCCCCCCCCCC	12.69	30206219
1955	Phosphorylation	SPTSPTYSLTSPAIS CCCCCCCCCCCCCCC	27.87	23663014
1957	Phosphorylation	TSPTYSLTSPAISPD CCCCCCCCCCCCCCC	27.07	30108239
1958	Phosphorylation	SPTYSLTSPAISPDD CCCCCCCCCCCCCCC	20.02	23663014
1962	Phosphorylation	SLTSPAISPDDSDEE CCCCCCCCCCCCCCC	25.12	19413330
1966	Phosphorylation	PAISPDDSDEEN--- CCCCCCCCCCCC---	55.06	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1525	T	Phosphorylation	Kinase	CDK9	P50750	PSP
1540	T	Phosphorylation	Kinase	CDK9	P50750	PSP
1616	S	Phosphorylation	Kinase	BRD4	O60885	PSP
1616	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
1616	S	Phosphorylation	Kinase	CDK9	P50750	PSP
1616	S	Phosphorylation	Kinase	CDK7	P50613	PSP
1616	S	Phosphorylation	Kinase	CDK13	Q14004	PSP
1616	S	Phosphorylation	Kinase	CDK12	Q9NYV4	PSP
1616	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
1618	T	Phosphorylation	Kinase	CDK9	P50750	PSP
1619	S	Phosphorylation	Kinase	CDK13	Q14004	PSP
1619	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
1619	S	Phosphorylation	Kinase	CDK7	P50613	PSP
1619	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
1619	S	Phosphorylation	Kinase	CDK12	Q9NYV4	PSP
1619	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
1619	S	Phosphorylation	Kinase	CDK9	P50750	PSP
1621	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
1621	S	Phosphorylation	Kinase	CDK9	P50750	PSP
1621	S	Phosphorylation	Kinase	CDK7	P50613	PSP
1878	S	Phosphorylation	Kinase	CDK7	P50613	PSP
1920	S	Phosphorylation	Kinase	CDK1	P06493	PSP
1934	S	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:15886201
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:17996703
-	K	Ubiquitination	E3 ubiquitin ligase	BARD1	Q99728	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	WWP2	O00308	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	S	Phosphorylation	23186163
Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9.
2	S	Phosphorylation	23186163
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
2	S	Acetylation	23186163
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
5	S	Methylation	31353023
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
5	S	Phosphorylation	31353023
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
5	S	Phosphorylation	31353023
Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9.
7	K	Methylation	26687004
Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.
7	S	Methylation	31353023
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
7	K	Phosphorylation	26687004
Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.
7	K	Phosphorylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
7	K	Methylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated.
7	K	Methylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated.
7	K	Acetylation	26687004
EP300 is one of the enzyme able to acetylate 'Lys-7'.
7	K	Acetylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
7	K	Acetylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated.
7	K	Acetylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated.
7	S	Phosphorylation	31353023
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
7	S	Phosphorylation	31353023
Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts.
1805	S	Methylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1805	S	Phosphorylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1808	S	Phosphorylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1808	S	Methylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Methylation	21454787
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Phosphorylation	21454787
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Methylation	21454787
Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RPB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED21_HUMAN	MED21	physical	9159119
CTDP1_HUMAN	CTDP1	physical	9159119
TF2B_HUMAN	GTF2B	physical	9159119
TBP_HUMAN	TBP	physical	9159119
TAF11_HUMAN	TAF11	physical	9159119
T2EA_HUMAN	GTF2E1	physical	9159119
T2FA_HUMAN	GTF2F1	physical	9159119
TF2H4_HUMAN	GTF2H4	physical	9159119
SMYD3_HUMAN	SMYD3	physical	15235609
TCEA1_HUMAN	TCEA1	physical	12914699
T2FA_HUMAN	GTF2F1	physical	9710619
CDK8_HUMAN	CDK8	physical	9710619
MED21_HUMAN	MED21	physical	9710619
SNF5_HUMAN	SMARCB1	physical	9710619
SMCA2_HUMAN	SMARCA2	physical	9710619
KAT2B_HUMAN	KAT2B	physical	9710619
TCRG1_HUMAN	TCERG1	physical	10908677
RPAB3_HUMAN	POLR2H	physical	9201987
RPAB5_HUMAN	POLR2L	physical	9201987
RPB3_HUMAN	POLR2C	physical	9201987
RPAB1_HUMAN	POLR2E	physical	9201987
RPB7_HUMAN	POLR2G	physical	9201987
RPAB2_HUMAN	POLR2F	physical	9201987
ELP3_HUMAN	ELP3	physical	11714725
PCIF1_HUMAN	PCIF1	physical	12565871
SPT5H_HUMAN	SUPT5H	physical	9450929
SND1_HUMAN	SND1	physical	12234934
T2FB_HUMAN	GTF2F2	physical	3860504
EGLN2_HUMAN	EGLN2	physical	18285459
EGLN1_HUMAN	EGLN1	physical	18285459
UB2L3_HUMAN	UBE2L3	physical	17996703
NEDD4_HUMAN	NEDD4	physical	17996703
RPB2_HUMAN	POLR2B	physical	19240132
RPB3_HUMAN	POLR2C	physical	19240132
RPAB1_HUMAN	POLR2E	physical	19240132
RPAB2_HUMAN	POLR2F	physical	19240132
RPB7_HUMAN	POLR2G	physical	19240132
RPAB3_HUMAN	POLR2H	physical	19240132
RPB9_HUMAN	POLR2I	physical	19240132
RPB11_HUMAN	POLR2J	physical	19240132
SPT6H_HUMAN	SUPT6H	physical	19141475
CTCF_HUMAN	CTCF	physical	17210645
DDX5_HUMAN	DDX5	physical	17011493
AGO1_HUMAN	AGO1	physical	16936726
KMT2A_HUMAN	KMT2A	physical	16199523
KMT2D_HUMAN	KMT2D	physical	16199523
MEN1_HUMAN	MEN1	physical	16199523
ITCH_HUMAN	ITCH	physical	16055720
NF1_HUMAN	NF1	physical	15999204
SMCA4_HUMAN	SMARCA4	physical	15999204
WAC_HUMAN	WAC	physical	21329877
SPT6H_MOUSE	Supt6	physical	17234882
CDK9_HUMAN	CDK9	physical	17234882
LEO1_HUMAN	LEO1	physical	20178742
PAF1_HUMAN	PAF1	physical	20178742
CDN1A_HUMAN	CDKN1A	physical	21088000
XRCC5_HUMAN	XRCC5	physical	12391174
ACTB_HUMAN	ACTB	physical	15502823
HIRA_HUMAN	HIRA	physical	22195966
CABIN_HUMAN	CABIN1	physical	22195966
UBN1_HUMAN	UBN1	physical	22195966
PHF8_HUMAN	PHF8	physical	20421419
SPT5H_HUMAN	SUPT5H	physical	21880767
SMC1A_HUMAN	SMC1A	physical	21880767
SMC3_HUMAN	SMC3	physical	21880767
CTCF_HUMAN	CTCF	physical	21880767
MCM3_HUMAN	MCM3	physical	21880767
MCM7_HUMAN	MCM7	physical	21880767
GTF2I_HUMAN	GTF2I	physical	21880767
PCNA_HUMAN	PCNA	physical	21880767
HNRPU_HUMAN	HNRNPU	physical	15711563
ACTB_HUMAN	ACTB	physical	15711563
BRNP1_HUMAN	BRINP1	physical	22446626
ZN326_HUMAN	ZNF326	physical	22446626
EWS_HUMAN	EWSR1	physical	20972445
EP300_HUMAN	EP300	physical	16916636
HMGN1_HUMAN	HMGN1	physical	16916636
ERCC6_HUMAN	ERCC6	physical	16916636
ERCC8_HUMAN	ERCC8	physical	16916636
DDB1_HUMAN	DDB1	physical	16916636
CSN1_HUMAN	GPS1	physical	16916636
XPF_HUMAN	ERCC4	physical	16916636
TCEA1_HUMAN	TCEA1	physical	16916636
SYF1_HUMAN	XAB2	physical	16916636
ERCC3_HUMAN	ERCC3	physical	16916636
ERCC5_HUMAN	ERCC5	physical	16916636
ERCC1_HUMAN	ERCC1	physical	16916636
XPA_HUMAN	XPA	physical	16916636
RFA1_HUMAN	RPA1	physical	16916636
YAP1_HUMAN	YAP1	physical	9305852
NEDD4_MOUSE	Nedd4	physical	9305852
YAP1_MOUSE	Yap1	physical	9305852
U2AF2_HUMAN	U2AF2	physical	21536736
PRP19_HUMAN	PRPF19	physical	21536736
CSTF1_HUMAN	CSTF1	physical	9002523
CSTF2_HUMAN	CSTF2	physical	9002523
CSTF3_HUMAN	CSTF3	physical	9002523
CPSF1_HUMAN	CPSF1	physical	9002523
CPSF3_HUMAN	CPSF3	physical	9002523
CPSF2_HUMAN	CPSF2	physical	9002523
TBP_HUMAN	TBP	physical	9002523
RPB1_HUMAN	POLR2A	physical	15282296
MYO6_HUMAN	MYO6	physical	16949370
RPB3_HUMAN	POLR2C	physical	22939629
RPB2_HUMAN	POLR2B	physical	22939629
RPB9_HUMAN	POLR2I	physical	22939629
RPB4_HUMAN	POLR2D	physical	22939629
SPT5H_HUMAN	SUPT5H	physical	22939629
T2FA_HUMAN	GTF2F1	physical	22939629
TCEA1_HUMAN	TCEA1	physical	22939629
RUVB2_HUMAN	RUVBL2	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
SPT5H_HUMAN	SUPT5H	physical	11940650
CSTF1_HUMAN	CSTF1	physical	11459828
CSTF1_RAT	Cstf1	physical	11459828
CSTF3_HUMAN	CSTF3	physical	11459828
TAT_HV1H2	tat	physical	11112772
T2AG_HUMAN	GTF2A2	physical	10454562
TF2H1_HUMAN	GTF2H1	physical	10454562
CSTF3_HUMAN	CSTF3	physical	10454562
CPSF3_HUMAN	CPSF3	physical	10454562
MCM2_HUMAN	MCM2	physical	10454562
MCM7_HUMAN	MCM7	physical	10454562
AGO1_HUMAN	AGO1	physical	24086155
IRF3_HUMAN	IRF3	physical	23994473
TF65_HUMAN	RELA	physical	23994473
MAP4_HUMAN	MAP4	physical	22863883
PP4R1_HUMAN	PPP4R1	physical	22863883
WDHD1_HUMAN	WDHD1	physical	22863883
ESR1_HUMAN	ESR1	physical	16957778
SRC_HUMAN	SRC	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
HNRPU_HUMAN	HNRNPU	physical	18710935
KAT2B_HUMAN	KAT2B	physical	18710935
ACTB_HUMAN	ACTB	physical	18710935
T2EB_HUMAN	GTF2E2	physical	26344197
T2FB_HUMAN	GTF2F2	physical	26344197
RPAB1_HUMAN	POLR2E	physical	26344197
RPAB2_HUMAN	POLR2F	physical	26344197
RPAB3_HUMAN	POLR2H	physical	26344197
RPB9_HUMAN	POLR2I	physical	26344197
RPB11_HUMAN	POLR2J	physical	26344197
RPAB5_HUMAN	POLR2L	physical	26344197
SRRT_HUMAN	SRRT	physical	26344197
SRSF2_HUMAN	SRSF2	physical	26344197
SPT4H_HUMAN	SUPT4H1	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
UBE3B_HUMAN	UBE3B	physical	26344197
CDK2_HUMAN	CDK2	physical	9311822
CCNH_HUMAN	CCNH	physical	9311822
CDK7_HUMAN	CDK7	physical	9311822
CPSF1_HUMAN	CPSF1	physical	9311784
TBP_HUMAN	TBP	physical	9311784
NSD1_HUMAN	NSD1	physical	25193115
SMN_HUMAN	SMN1	physical	26700805
ANM5_HUMAN	PRMT5	physical	26700805
XRN2_HUMAN	XRN2	physical	26700805
SETX_HUMAN	SETX	physical	26700805
TDRD3_HUMAN	TDRD3	physical	26700805
TERA_HUMAN	VCP	physical	28036256

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RPB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-1839; THR-1840; THR-1842; SER-1843; SER-1845;SER-1847; SER-1849; SER-1850; TYR-1853; SER-1857; SER-1871; TYR-1874;SER-1875; THR-1877; SER-1878; TYR-1881; SER-1882; THR-1884; TYR-1888;SER-1889; SER-1892; THR-1894; TYR-1895; SER-1896; THR-1898; SER-1899;TYR-1902; THR-1903; SER-1906; TYR-1909; SER-1917; TYR-1923; SER-1924;THR-1926; SER-1927; THR-1929; TYR-1930; SER-1931; THR-1933; SER-1934;SER-1962 AND SER-1966, AND MASS SPECTROMETRY.	19413330 [Abstract]
Methylation
Reference	PubMed
"The C-terminal domain of RNA polymerase II is modified by site-specific methylation."; Sims R.J. III, Rojas L.A., Beck D., Bonasio R., Schuller R.,Drury W.J. III, Eick D., Reinberg D.; Science 332:99-103(2011). Cited for: METHYLATION AT ARG-1810 BY CARM1, AND MUTAGENESIS OF ARG-1810.	21454787 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1815; SER-1843;TYR-1853; THR-1854; TYR-1874; SER-1878; SER-1882; SER-1899; TYR-1909;SER-1913; SER-1917; THR-1919 AND SER-1920, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-1839; THR-1840; THR-1842; SER-1843; SER-1845;SER-1847; SER-1849; SER-1850; TYR-1853; SER-1857; SER-1871; TYR-1874;SER-1875; THR-1877; SER-1878; TYR-1881; SER-1882; THR-1884; TYR-1888;SER-1889; SER-1892; THR-1894; TYR-1895; SER-1896; THR-1898; SER-1899;TYR-1902; THR-1903; SER-1906; TYR-1909; SER-1917; TYR-1923; SER-1924;THR-1926; SER-1927; THR-1929; TYR-1930; SER-1931; THR-1933; SER-1934;SER-1962 AND SER-1966, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1849; TYR-1874;THR-1891; SER-1896; TYR-1923; SER-1927 AND SER-1934, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772 AND SER-777, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1896 AND SER-1934, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY.	15592455 [Abstract]

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show